Recombinant Human Calpain-2 Catalytic Subunit (CAPN2) Protein (His)

Name: Recombinant Human Calpain-2 Catalytic Subunit (CAPN2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03136P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Calpain-2 Catalytic Subunit (CAPN2) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P17655
Target Symbol	CAPN2
Synonyms	Calcium activated neutral proteinase 2; Calcium activated neutral proteinase; Calcium-activated neutral protease 2; catalytic subunit; Calcium-activated neutral proteinase 2; CALP80; Calpain 2 (m/II) large subunit; Calpain 2 catalytic subunit; Calpain 2 large catalytic subunit; Calpain 2 large subunit; Calpain 2; large [catalytic] subunit; Calpain large polypeptide L2; Calpain M type; Calpain M-type; Calpain-2 catalytic subunit; Calpain-2 large subunit; Calpain2; CAN2_HUMAN; CANP 2; CANP L2; CANP2; CANPL 2; CANPL2; CANPml; Capa2; CAPN 2; CAPN2; FLJ39928; M calpain; M calpin; M type; M-calpain; mCANP; Millimolar calpain; Millimolar-calpain
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	SHDRAIKYLNQDYEALRNECLEAGTLFQDPSFPAIPSALGFKELGPYSSKTRGIEWKRPTEICADPQFIIGGATRTDICQGALGDCWLLAAIASLTLNEEILARVVPLNQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEGSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELKKPPPNLFKIIQKALQKGSLLGCSIDITSAADSEAITFQKLVKGHAYSVTGAEEVESNGSLQKLIRIRNPWGEVEWTGRWNDNCPSWNTIDPEERERLTRRHEDGEFWMSFSDFLRHYSRLEICNLTPDTLTSDTYKKWKLTKMDGNWRRGSTAGGCRNYPNTFWMNPQYLIKLEEEDEDEEDGESGCTFLVGLIQKHRRRQRKMGEDMHTIGFGIYEVPEELSGQTNIHLSKNFFLTNRARERSDTFINLREVLNRFKLPPGEYILVPSTFEPNKDGDFCIRVFSEKKADYQAVDDEIEANLEEFDISEDDIDDGFRRLFAQLAGEDAEISAFELQTILRRVLAKRQDIKSDGFSIETCKIMVDMLDSDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSYEMRKALEEAGFKMPCQLHQVIVARFADDQLIIDFDNFVRCLVRLETLFKIFKQLDPENTGTIELDLISWLCFSVL
Expression Range	20-700aa
Protein Length	Full Length of Mature Protein
Mol. Weight	82.1kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Calcium-regulated non-lysosomal thiol-protease which catalyzes limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction. Proteolytically cleaves MYOC at 'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs.
Subcellular Location	Cytoplasm. Cell membrane. Note=Translocates to the plasma membrane upon Ca(2+) binding.
Protein Families	Peptidase C2 family
Database References	HGNC: 1479 OMIM: 114230 KEGG: hsa:824 STRING: 9606.ENSP00000295006 UniGene: PMID: 30106446 in the field of neural injury, calpain-2 and caspase-3 proteases generate breakdown-products (BDPs) fragments that are indicative of different neural cell death mechanisms in different injury scenarios. Advanced proteomic techniques have shown a remarkable progress in identifying these BDPs experimentally PMID: 28112201 The results of the present study suggested that miR93 regulated MMP1 and collagen I expression in fibroblasts via calpain2. miR93 mediated collagen expression in stress urinary incontinence via calpain2. PMID: 29115452 Hyperactivated m-calpain induced cytoplasmic accumulation of truncated topoisomerase IIalpha in doxorubicin resistant T47D cells. PMID: 29425806 Results find that overexpression of hTau increases intracellular calcium, which in turn activates calpain-2 and induces degradation of alpha4 nAChR. PMID: 27277673 m-calpain translocated as the result of calcium influx was involved in DNA double-strand breaks repair, especially in the non-homologous end-joining pathway through proteolysis of nuclear Ku80. Cleaved Ku80 was still able to form a heterodimer with Ku70 and enhance DNA repair activity. PMID: 27121057 3 novel loci associated with serum alpha-carotene concentrations among a population that consumed a controlled diet. While replication is necessary, the CAPN2/CAPN8 locus provides compelling evidence for an association with serum alpha-carotene concentrations and may suggest a relationship with the development and progression of cancers. PMID: 28002826 The inhibitory effects of BMP4 on PDGF-induced cell proliferation, collagen synthesis, and calpain-2 activation are impaired in pulmonary artery smooth muscle cells from pulmonary arterial hypertension patient. PMID: 28235949 Calpain-2 upregulates PDGF-induced Akt phosphorylation in pulmonary vascular remodeling via an intracrine TGF-beta1/mTORC2 mechanism. PMID: 27099352 the expression of CAPN2 was elevated in prostate cancer tissues than that in normal control tissues. PMID: 28280729 Calpain 2-mediated cleavage of Atg3 and Atg7 accounts for the impaired autophagy. PMID: 27077802 Calcineurin together with its upstream molecule, calpain 2, and its downstream effector, NFAT-c3, might contribute to the development of atrial fibrillation in patients with heart valve disease and diabetes. PMID: 27123462 Calpain-2 modulates pulmonary vascular remodeling in pulmonary arterial hypertension. PMID: 26248159 Taken together, our results demonstrated the deregulation of GAS2 in both AML and ALL and the requirement of GAS2-Calpain2 axis for the growth of leukemic cells. PMID: 26358320 The combination of Ca2+ and ionomycin was required to activate calpain 2, resulting in the further degradation of Dicer and the appearance of a degradation product similar to that detected in platelets from some diabetic individuals. PMID: 25944670 In a transgenic mouse model, hypoxia-triggered m-calpain activation is involved in endoplasmic reticulum stress-mediated Alzheimer's disease pathogenesis. PMID: 23889979 Small interfering RNA (siRNA)-mediated silencing of m-calpain expression significantly suppressed the adhesive, migrative and invasive potentials of human hepatoma cells. PMID: 23733271 The data reveal that hGAAP is a novel regulator of focal adhesion dynamics, cell adhesion, and migration by controlling localized Ca(2+)-dependent activation of calpain 2. PMID: 23940116 The carboxyl tail of alpha-actinin-4 regulates its susceptibility to m-calpain and thus functions in cell migration and spreading. PMID: 23466492 data demonstrate that GSK-3beta plays an important role in regulating tRXRalpha production by calpain II in cancer cells PMID: 23389291 alpha-II spectrin was drastically accumulated in infected T cells derived from adult T-cell leukemia patients, whereas its digestive protease calpain-2 (CAN2) was significantly downregulated. PMID: 23538341 The results suggest that calpain-2 and calpastatin expression is important in pancreatic cancers, influencing disease progression PMID: 23140395 High expression of calpain-2 is significantly associated with resistance to platinum-based adjuvant chemotherapy. PMID: 22435971 Expression of the large catalytic subunit of calpain-2 is significantly associated with clinical outcome of patients with triple-negative and basal-like disease. PMID: 22745213 betaig-h3 co-localized with integrin alpha5beta1 to enhance the invasion of U87 cells, and that calpain-2, is involved in this process, acting as a downstream molecule. PMID: 22629380 Two human hepatocellular carcinoma cell lines were researched using proteomics. A proteolysis network was built up, of which the CAPN2 centered subnetwork, including SPTBN1, ATP5B, and VIM, was more active in the highly metastatic HCC cell line. PMID: 22623320 cleavage of CPEB3 by NMDA-activated calpain 2 accounts for the activity-related translation of CPEB3-targeted RNAs PMID: 22711986 Staining intensity of calpain 2 in ovarian carcinoma decreased with increasing lymph node status. PMID: 22335024 Subtype-selective induction of m-calpain in aorta during atherosclerotic progression is associated with proteolytic disorganization of VE-cadherin and proatherogenic hyperpermeability in cells. PMID: 22064597 The expression of m-calpain-induced degradation products of extracellular matrix was correlated with the degree of disc degeneration in human intervertebral disc tissue PMID: 21839844 Data show that transfection of cells with GRP78 or calpain I and calpain II siRNA reduced MPTB-mediated cell apoptosis in chondrosarcoma JJ012 cells. PMID: 21374734 Calpain 2-mediated hTOP1 proteolysis not only impacts its biochemical activities but also alters some cellular functions of hTOP1. PMID: 21086148 Confocal immunostaining demonstrated colocalization of m-calpain and the aggrecan product within the lower hypertrophic chondrocytes and in limited region of the pericellular matrix. PMID: 21117903 NHE1 might participate in HIF-1-induced angiogenesis due, at least in part, to the alteration of calpain activity. PMID: 21185840 Findings support the idea that calpain is involved in the turnover of LFA-1 adhesions at the rear of the cell. PMID: 21152086 In brain, calpain-2 plays critical roles in developmental and adult synaptic plasticity. PMID: 20924799 Knockdown of calpain 2 expression using shRNA or chemical inhibition of calpain activity reduced glioblastoma cell invasion by 90%. PMID: 20730561 m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. PMID: 20729206 Data indicate that calpains are involved in the C-terminal truncation of aggrecan and might have a minor role in arthritic diseases. PMID: 20618160 High m-calpain expression is associated with rhabdomyosarcoma aggressiveness. PMID: 20193680 Overexpression of calpain-2 and low expression of calpastatin may involve in the pathological development of stress urinary incontinence. PMID: 19756344 analysis of a novel role for calpain proteolysis of FAK in regulating adhesion dynamics in motile cells PMID: 20150423 excessive TRPM7 channel activity causes oxidative and nitrosative stresses, producing cell rounding mediated by p38 MAPK/JNK-dependent activation of m-calpain PMID: 20070945 m-Calpain antagonizes RhoA overactivation and endothelial barrier dysfunction under disturbed shear conditions. PMID: 19752040 a higher calpain/calpastatin ratio collaborates with activated ERK to promote the generation of the low molecular weight-AR PMID: 19946123 Overactivation of Ca(2+)-calpain pathways contributes to beta cell dysfunction and apoptosis in type 2 diabetes. PMID: 19861418 Calpain activation in neurodegenerative diseases PMID: 12070670 colocalization with detergent-insoluble rafts on T-cells PMID: 12150984 localization of m-calpain within caveolae may contribute to maintenance of the enzyme in an inactive state and that m-calpain may also contribute to the regulation of calcium-sensing receptor levels. PMID: 12783889 activation of m-calpain during mitosis is required for cells to establish the chromosome alignment by regulating some molecules that generate polar ejection force PMID: 14688278

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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